SARA_STRGC
ID SARA_STRGC Reviewed; 663 AA.
AC P31306; A8AYX4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Oligopeptide-binding protein SarA;
DE AltName: Full=76 kDa cell surface lipoprotein;
DE Flags: Precursor;
GN Name=sarA; Synonyms=hppA; OrderedLocusNames=SGO_1712;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, DIACYLGLYCEROL AT CYS-23, AND
RP PALMITOYLATION AT CYS-23.
RX PubMed=1339408; DOI=10.1128/iai.60.3.1225-1228.1992;
RA Jenkinson H.F.;
RT "Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii
RT associated with expression of cell surface lipoproteins.";
RL Infect. Immun. 60:1225-1228(1992).
CC -!- FUNCTION: May be involved in the expression of cell surface properties
CC important for colonization of the human oral cavity. It may also be
CC involved in uptake processes.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; CP000725; ABV10882.1; -; Genomic_DNA.
DR EMBL; S85398; AAB21606.1; -; Genomic_DNA.
DR PIR; A43896; A43896.
DR RefSeq; WP_012130757.1; NC_009785.1.
DR AlphaFoldDB; P31306; -.
DR SMR; P31306; -.
DR STRING; 467705.SGO_1712; -.
DR EnsemblBacteria; ABV10882; ABV10882; SGO_1712.
DR KEGG; sgo:SGO_1712; -.
DR eggNOG; COG4166; Bacteria.
DR HOGENOM; CLU_026497_0_0_9; -.
DR OMA; HFINNGA; -.
DR Proteomes; UP000001131; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProt.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Peptide transport;
KW Protein transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT CHAIN 23..663
FT /note="Oligopeptide-binding protein SarA"
FT /id="PRO_0000018189"
FT REGION 637..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:1339408"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:1339408"
SQ SEQUENCE 663 AA; 73371 MW; EBCEAC3F7077BEE3 CRC64;
MKKGKILALA GVALLATGVL AACSNSTSNS SNSSSSGADQ VFNYIYEVDP ENLNYLISSK
AATTDLTANL IDGLLENDNY GNLVPSMAED WTVSKDGLTY TYTLRKDAKW YTSDGEEYAD
VKAQDFVAGL KYAADNKSET LYLVQSSIKG LDDYVNGKTK DFSSVGVKAV DDHTVQYTLN
EPESFWNSKT TMGILYPVNE EFLKSKGDKF AQSADPTSLL YNGPFLLKSI TSKSSIEFAK
NPNYWDKDNV HVSDVKLTYF DGQDQGKPAE QFAKGALSAA RLAPTSATFS KVEKEFKDNI
VYTPQDSTSY LVGVNIDRQA YNHTAKSSDA QKSSTKKALM NKDFRQALSF AFDRTAYASQ
VNGKEGATKM LRNLYIPPTF VQADGKSFGE LVKEKVASYG DEWKDVNFDD AQDGLYNKEK
AKAEFAKAKK ALQEEGVEFP IHLDMPVDQT ATAKVQRVQS LKQSIESSLG TDNVVVDIHQ
MKTDDVLNIT YYAASAAEED WDISDNVGWS PDYQDPSTYL EIIKPGGENT KTFLGFDGKE
NAAAEQVGLK EYAKLVDEAA AEKTDVNKRY EKYATAQAWL TDSALLIPTT SRTGRPVLTK
IVPFTAPFAW SGAKGRDMAS YKYLKLQDKA VTAKEYQKAQ EKWNKERAES NKKAQEELEK
HVK